besselj(j, ω) function Search Results


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Mimetics mimetics m2
(A) Atomic representation of the model of the complex between IL-10 (gray, PDB ID 1J7V) and the helical scaffold used in the rationale for the design of IL-10R1 mimetics (green, N -terminal <t>functionalization</t> in yellow). For clarity, no side chains shown for IL-10 Q38 and IL-10 L48 . (B) Snapshot of complex IL-10/M1 (at 2.9 ns from 10 ns MD simulation). (C) Snapshot of complex IL-10/M4 (at 10 ns). (D) Snapshot of complex IL-10/M6 (at 3.6 ns). Residues involved in recognition are shown in sticks and colored by atom type (IL-10 highlighted in violet in A). Red spheres represent interfacial structural waters observed during MD simulations. Intermolecular H-bonds are depicted by black dashed lines. Figure generated in PyMOL .
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Accelrys dmol3 package
(A) Atomic representation of the model of the complex between IL-10 (gray, PDB ID 1J7V) and the helical scaffold used in the rationale for the design of IL-10R1 mimetics (green, N -terminal <t>functionalization</t> in yellow). For clarity, no side chains shown for IL-10 Q38 and IL-10 L48 . (B) Snapshot of complex IL-10/M1 (at 2.9 ns from 10 ns MD simulation). (C) Snapshot of complex IL-10/M4 (at 10 ns). (D) Snapshot of complex IL-10/M6 (at 3.6 ns). Residues involved in recognition are shown in sticks and colored by atom type (IL-10 highlighted in violet in A). Red spheres represent interfacial structural waters observed during MD simulations. Intermolecular H-bonds are depicted by black dashed lines. Figure generated in PyMOL .
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Image Search Results


(A) Atomic representation of the model of the complex between IL-10 (gray, PDB ID 1J7V) and the helical scaffold used in the rationale for the design of IL-10R1 mimetics (green, N -terminal functionalization in yellow). For clarity, no side chains shown for IL-10 Q38 and IL-10 L48 . (B) Snapshot of complex IL-10/M1 (at 2.9 ns from 10 ns MD simulation). (C) Snapshot of complex IL-10/M4 (at 10 ns). (D) Snapshot of complex IL-10/M6 (at 3.6 ns). Residues involved in recognition are shown in sticks and colored by atom type (IL-10 highlighted in violet in A). Red spheres represent interfacial structural waters observed during MD simulations. Intermolecular H-bonds are depicted by black dashed lines. Figure generated in PyMOL .

Journal: PLoS ONE

Article Title: Rational Structure-Based Rescaffolding Approach to De Novo Design of Interleukin 10 (IL-10) Receptor-1 Mimetics

doi: 10.1371/journal.pone.0154046

Figure Lengend Snippet: (A) Atomic representation of the model of the complex between IL-10 (gray, PDB ID 1J7V) and the helical scaffold used in the rationale for the design of IL-10R1 mimetics (green, N -terminal functionalization in yellow). For clarity, no side chains shown for IL-10 Q38 and IL-10 L48 . (B) Snapshot of complex IL-10/M1 (at 2.9 ns from 10 ns MD simulation). (C) Snapshot of complex IL-10/M4 (at 10 ns). (D) Snapshot of complex IL-10/M6 (at 3.6 ns). Residues involved in recognition are shown in sticks and colored by atom type (IL-10 highlighted in violet in A). Red spheres represent interfacial structural waters observed during MD simulations. Intermolecular H-bonds are depicted by black dashed lines. Figure generated in PyMOL .

Article Snippet: Thus, based on the structure of the refined model of the M1 /IL-10 complex ( ) and taking into account the interaction energies obtained with the sp 3 and sp 2 amine cation chemical probes ( vide supra ), two new mimetics ( M2 , M3 ; differing in tryptophan vs . its 5-hydroxy derivative in position 2) were designed by N-terminal functionalization with 4-guanidinobutanoyl, providing a positively charged H-bond donor for potential interaction with the negatively charged side chain of IL-10 E50 (helix B).

Techniques: Generated